ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 9 citations in OpenAlex.
- Inter-domain communication in the dimeric DEAD-box helicase Hera from T. thermophilus and implications for the mechanism of RNA unwinding.Nucleic acids research · 2025Article
- TheRNA (New York, N.Y.) · 2020Article
- DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition.Nucleic acids research · 2014Article
- Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera.Nucleic acids research · 2013Article
- The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core.RNA (New York, N.Y.) · 2009Article
- A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.Nucleic acids research · 2009Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-resistant RNA-dependent ATPase (Hera) from Thermus thermophilus is a DEAD-box RNA helicase. Two constructs encompassing the second RecA-like domain and the C-terminal domain of Hera were overproduced in Escherichia coli and purified to homogeneity. Single crystals of both Hera constructs were obtained in three crystal forms. A tetragonal crystal form belonged to space group P4(1)2(1)2, with unit-cell parameters a = 65.5, c = 153.0 A, and contained one molecule per asymmetric unit. Two orthorhombic forms belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 62.8, b = 70.9, c = 102.3 A (form I) and a = 41.6, b = 67.6, c = 183.5 A (form II). Both orthorhombic forms contained two molecules per asymmetric unit. All crystals diffracted X-rays to beyond 3 A resolution, but the tetragonal data sets displayed high Wilson B values and high mean |E(2) - 1| values, indicating potential disorder and anisotropy. The tetragonal crystal was phased by MAD using a single selenium site.
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